Literature DB >> 24403057

Mechanisms for regulating deubiquitinating enzymes.

Cynthia Wolberger1.   

Abstract

Ubiquitination is a reversible post-translational modification that plays a dynamic role in regulating most eukaryotic processes. Deubiquitinating enzymes (DUBs), which hydrolyze the isopeptide or peptide linkages joining ubiquitin to substrate lysines or N-termini, therefore play a key role in ubiquitin signaling. Cells employ multiple mechanisms to regulate DUB activity and thus ensure the appropriate biological response. Recent structural studies have shed light on several different mechanisms by which DUB activity and specificity is regulated.
© 2014 The Protein Society.

Entities:  

Keywords:  DUB; UBL; deubiquitinating enzymes; ubiquitin

Mesh:

Substances:

Year:  2014        PMID: 24403057      PMCID: PMC3970886          DOI: 10.1002/pro.2415

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


  73 in total

1.  Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair.

Authors:  R M Hofmann; C M Pickart
Journal:  Cell       Date:  1999-03-05       Impact factor: 41.582

Review 2.  The WD40-repeat protein-containing deubiquitinase complex: catalysis, regulation, and potential for therapeutic intervention.

Authors:  Mark A Villamil; Qin Liang; Zhihao Zhuang
Journal:  Cell Biochem Biophys       Date:  2013-09       Impact factor: 2.194

3.  Crystal structure of a Josephin-ubiquitin complex: evolutionary restraints on ataxin-3 deubiquitinating activity.

Authors:  Stephen D Weeks; Kimberly C Grasty; Lisa Hernandez-Cuebas; Patrick J Loll
Journal:  J Biol Chem       Date:  2010-11-30       Impact factor: 5.157

4.  Two isoforms of otubain 1 regulate T cell anergy via GRAIL.

Authors:  Luis Soares; Christine Seroogy; Heidi Skrenta; Niroshana Anandasabapathy; Patricia Lovelace; Chan D Chung; Edgar Engleman; C Garrison Fathman
Journal:  Nat Immunol       Date:  2003-12-07       Impact factor: 25.606

5.  Structural basis for assembly and activation of the heterotetrameric SAGA histone H2B deubiquitinase module.

Authors:  Alwin Köhler; Erik Zimmerman; Maren Schneider; Ed Hurt; Ning Zheng
Journal:  Cell       Date:  2010-04-29       Impact factor: 41.582

6.  OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis.

Authors:  Tycho E T Mevissen; Manuela K Hospenthal; Paul P Geurink; Paul R Elliott; Masato Akutsu; Nadia Arnaudo; Reggy Ekkebus; Yogesh Kulathu; Tobias Wauer; Farid El Oualid; Stefan M V Freund; Huib Ovaa; David Komander
Journal:  Cell       Date:  2013-07-03       Impact factor: 41.582

7.  Reversible inactivation of deubiquitinases by reactive oxygen species in vitro and in cells.

Authors:  Jin-Gu Lee; Kheewoong Baek; Nia Soetandyo; Yihong Ye
Journal:  Nat Commun       Date:  2013       Impact factor: 14.919

8.  The mechanism of OTUB1-mediated inhibition of ubiquitination.

Authors:  Reuven Wiener; Xiangbin Zhang; Tao Wang; Cynthia Wolberger
Journal:  Nature       Date:  2012-02-22       Impact factor: 49.962

9.  Ube2W conjugates ubiquitin to α-amino groups of protein N-termini.

Authors:  Michael H Tatham; Anna Plechanovová; Ellis G Jaffray; Helena Salmen; Ronald T Hay
Journal:  Biochem J       Date:  2013-07-01       Impact factor: 3.857

10.  Regulation of A20 and other OTU deubiquitinases by reversible oxidation.

Authors:  Yogesh Kulathu; Francisco J Garcia; Tycho E T Mevissen; Martin Busch; Nadia Arnaudo; Kate S Carroll; David Barford; David Komander
Journal:  Nat Commun       Date:  2013       Impact factor: 14.919

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  16 in total

Review 1.  Ubiquitin, the centrosome, and chromosome segregation.

Authors:  Ying Zhang; Paul J Galardy
Journal:  Chromosome Res       Date:  2016-01       Impact factor: 5.239

2.  Recruitment and allosteric stimulation of a histone-deubiquitinating enzyme during heterochromatin assembly.

Authors:  Alexis Zukowski; Nouf Omar Al-Afaleq; Emily D Duncan; Tingting Yao; Aaron M Johnson
Journal:  J Biol Chem       Date:  2017-12-29       Impact factor: 5.157

3.  Uncovering the role of Sgf73 in maintaining SAGA deubiquitinating module structure and activity.

Authors:  Ming Yan; Cynthia Wolberger
Journal:  J Mol Biol       Date:  2014-12-17       Impact factor: 5.469

4.  OTUD4 Is a Phospho-Activated K63 Deubiquitinase that Regulates MyD88-Dependent Signaling.

Authors:  Yu Zhao; Miranda C Mudge; Jennifer M Soll; Rachel B Rodrigues; Andrea K Byrum; Elizabeth A Schwarzkopf; Tara R Bradstreet; Steven P Gygi; Brian T Edelson; Nima Mosammaparast
Journal:  Mol Cell       Date:  2018-02-01       Impact factor: 17.970

5.  Phosphorylated E2F1 is stabilized by nuclear USP11 to drive Peg10 gene expression and activate lung epithelial cells.

Authors:  Dan Wang; Jing Zhao; Shuang Li; Jianxin Wei; Ling Nan; Rama K Mallampalli; Nathaniel M Weathington; Haichun Ma; Yutong Zhao
Journal:  J Mol Cell Biol       Date:  2018-02-01       Impact factor: 6.216

Review 6.  Substrate specificity of the ubiquitin and Ubl proteases.

Authors:  Judith A Ronau; John F Beckmann; Mark Hochstrasser
Journal:  Cell Res       Date:  2016-03-25       Impact factor: 25.617

Review 7.  The business of deubiquitination - location, location, location.

Authors:  Erin S Coyne; Simon S Wing
Journal:  F1000Res       Date:  2016-02-11

Review 8.  Proteostasis, oxidative stress and aging.

Authors:  Ioanna Korovila; Martín Hugo; José Pedro Castro; Daniela Weber; Annika Höhn; Tilman Grune; Tobias Jung
Journal:  Redox Biol       Date:  2017-07-12       Impact factor: 11.799

9.  Oxygen-dependent bond formation with FIH regulates the activity of the client protein OTUB1.

Authors:  Christina Pickel; Julia Günter; Amalia Ruiz-Serrano; Patrick Spielmann; Jacqueline-Alba Fabrizio; Witold Wolski; Daniel J Peet; Roland H Wenger; Carsten C Scholz
Journal:  Redox Biol       Date:  2019-07-02       Impact factor: 11.799

10.  A mobile loop near the active site acts as a switch between the dual activities of a viral protease/deubiquitinase.

Authors:  Isabelle Jupin; Maya Ayach; Lucile Jomat; Sonia Fieulaine; Stéphane Bressanelli
Journal:  PLoS Pathog       Date:  2017-11-08       Impact factor: 6.823

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